![]() |
|
Annotation rule MF_00117 |
Accession | MF_00117 |
Dates | 1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 20) |
Name | HslO |
Scope | Bacteria |
Template | P0A6Y5 (HSLO_ECOLI) |
Triggered by |
Identifier |
|
Protein name |
|
Gene name |
|
Function | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. |
Subcellular location | Cytoplasm. |
Ptm | Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive. |
Similarity | Belongs to the HSP33 family. |
Pfam | PF01430; HSP33; 1; |
From: HSLO_ECOLI (P0A6Y5) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DISULFID | 230 | 232 | Redox-active | C-x-C | ||||||||
DISULFID | 263 | 266 | Redox-active | C-x(2)-C |
Size range | 281-341 amino acids |
Related rules | None |
Fusion | None |
Comments | Possible wrong start in AQUAE and DEIRA |